ID UVRC_THEMA Reviewed; 557 AA.
AC Q9WYA3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=UvrABC system protein C {ECO:0000255|HAMAP-Rule:MF_00203};
DE Short=Protein UvrC {ECO:0000255|HAMAP-Rule:MF_00203};
DE AltName: Full=Excinuclease ABC subunit C {ECO:0000255|HAMAP-Rule:MF_00203};
GN Name=uvrC {ECO:0000255|HAMAP-Rule:MF_00203}; OrderedLocusNames=TM_0265;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC processing of DNA lesions. UvrC both incises the 5' and 3' sides of the
CC lesion. The N-terminal half is responsible for the 3' incision and the
CC C-terminal half is responsible for the 5' incision. {ECO:0000255|HAMAP-
CC Rule:MF_00203}.
CC -!- SUBUNIT: Interacts with UvrB in an incision complex.
CC {ECO:0000255|HAMAP-Rule:MF_00203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}.
CC -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000255|HAMAP-
CC Rule:MF_00203}.
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DR EMBL; AE000512; AAD35353.1; -; Genomic_DNA.
DR PIR; H72400; H72400.
DR RefSeq; NP_228078.1; NC_000853.1.
DR RefSeq; WP_004082969.1; NZ_CP011107.1.
DR PDB; 1YCZ; X-ray; 1.80 A; A=1-96.
DR PDB; 1YD0; X-ray; 1.50 A; A=1-96.
DR PDB; 1YD1; X-ray; 1.80 A; A=1-96.
DR PDB; 1YD2; X-ray; 1.60 A; A=1-96.
DR PDB; 1YD3; X-ray; 1.60 A; A=1-96.
DR PDB; 1YD4; X-ray; 1.90 A; A=1-96.
DR PDB; 1YD5; X-ray; 1.80 A; A=1-96.
DR PDB; 2NRR; X-ray; 1.20 A; A=345-502.
DR PDB; 2NRT; X-ray; 1.50 A; A=339-557.
DR PDB; 2NRV; X-ray; 1.80 A; A/B=339-557.
DR PDB; 2NRW; X-ray; 2.30 A; A=339-557.
DR PDB; 2NRX; X-ray; 1.90 A; A/B=339-557.
DR PDB; 2NRZ; X-ray; 2.00 A; A/B=339-557.
DR PDBsum; 1YCZ; -.
DR PDBsum; 1YD0; -.
DR PDBsum; 1YD1; -.
DR PDBsum; 1YD2; -.
DR PDBsum; 1YD3; -.
DR PDBsum; 1YD4; -.
DR PDBsum; 1YD5; -.
DR PDBsum; 2NRR; -.
DR PDBsum; 2NRT; -.
DR PDBsum; 2NRV; -.
DR PDBsum; 2NRW; -.
DR PDBsum; 2NRX; -.
DR PDBsum; 2NRZ; -.
DR AlphaFoldDB; Q9WYA3; -.
DR SMR; Q9WYA3; -.
DR STRING; 243274.TM_0265; -.
DR PaxDb; 243274-THEMA_03400; -.
DR EnsemblBacteria; AAD35353; AAD35353; TM_0265.
DR KEGG; tma:TM0265; -.
DR eggNOG; COG0322; Bacteria.
DR InParanoid; Q9WYA3; -.
DR OrthoDB; 9804933at2; -.
DR EvolutionaryTrace; Q9WYA3; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006974; P:DNA damage response; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd10434; GIY-YIG_UvrC_Cho; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.1440.10; GIY-YIG endonuclease; 1.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR Gene3D; 3.30.420.340; UvrC, RNAse H endonuclease domain; 1.
DR HAMAP; MF_00203; UvrC; 1.
DR InterPro; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR047296; GIY-YIG_UvrC_Cho.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR001943; UVR_dom.
DR InterPro; IPR036876; UVR_dom_sf.
DR InterPro; IPR004791; UvrC.
DR InterPro; IPR001162; UvrC_RNase_H_dom.
DR InterPro; IPR038476; UvrC_RNase_H_dom_sf.
DR NCBIfam; TIGR00194; uvrC; 1.
DR PANTHER; PTHR30562:SF1; UVRABC SYSTEM PROTEIN C; 1.
DR PANTHER; PTHR30562; UVRC/OXIDOREDUCTASE; 1.
DR Pfam; PF01541; GIY-YIG; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF08459; UvrC_RNaseH_dom; 1.
DR SMART; SM00465; GIYc; 1.
DR SUPFAM; SSF46600; C-terminal UvrC-binding domain of UvrB; 1.
DR SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
DR PROSITE; PS50151; UVR; 1.
DR PROSITE; PS50165; UVRC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW Excision nuclease; Reference proteome; SOS response.
FT CHAIN 1..557
FT /note="UvrABC system protein C"
FT /id="PRO_0000138354"
FT DOMAIN 14..89
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 194..229
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:1YD0"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1YD0"
FT STRAND 26..35
FT /evidence="ECO:0007829|PDB:1YD0"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:1YD0"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1YD0"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:1YD0"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1YD0"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:1YD0"
FT HELIX 346..353
FT /evidence="ECO:0007829|PDB:2NRR"
FT STRAND 362..369
FT /evidence="ECO:0007829|PDB:2NRR"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:2NRT"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:2NRR"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2NRR"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:2NRR"
FT HELIX 405..417
FT /evidence="ECO:0007829|PDB:2NRR"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:2NRR"
FT HELIX 432..444
FT /evidence="ECO:0007829|PDB:2NRR"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:2NRR"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:2NRT"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:2NRR"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:2NRR"
FT HELIX 475..492
FT /evidence="ECO:0007829|PDB:2NRR"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:2NRT"
FT HELIX 496..508
FT /evidence="ECO:0007829|PDB:2NRT"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:2NRW"
FT HELIX 516..526
FT /evidence="ECO:0007829|PDB:2NRT"
FT HELIX 529..533
FT /evidence="ECO:0007829|PDB:2NRT"
FT HELIX 537..544
FT /evidence="ECO:0007829|PDB:2NRT"
FT HELIX 547..556
FT /evidence="ECO:0007829|PDB:2NRT"
SQ SEQUENCE 557 AA; 64821 MW; 16B7F10C99212892 CRC64;
MKEKIRKKIL LAPEEPGVYI FKNKGVPIYI GKAKRLSNRL RSYLNPQTEK VFRIGEEADE
LETIVVMNER EAFILEANLI KKYRPKYNVR LKDTDFYPYI RISDDEIPYV EIVKRKLWDG
TYFGPYTSVQ FVRNLLEILQ KIMGFRTCKS DLKRIKRPCF LYHLGRCIGP CIGNIESHEE
AIRKLREFLS GNMEEVFDYL KEKMETHSKM LDFENAAKYR DLLLNLSNVL ESQGVVFEEN
INCDVLVHAH DLFVVLRVRN GYLVGKISFE MEGGNVEDFI REYYISGRGD IPKTLILESD
LDEMDYSSLG FEYVGPPRST TEEDLLEKAK KNLENELKMR GLRKEALEEL MKLLNMKDFP
YRIEGIDISH LQGKYTVASL VVFEDGFPKK GDYRRYKIEQ DHPDDYESIR TVVKRRYSKH
PLPNLLFVDG GIGQVNAAIE ALKEIGKDCP VVGLAKKEET VVFENREIHL PHDHPVLRLL
VQIRDETHRF AVSYHRKRRE KESLRSVLDN VPGIGPIRKK KLIEHFGSLE NIRSASLEEI
ARVIGSTEIA RRVLDIL
//
